A study of salmon ( Oncorhynchus tschawytscha ) pituitary gonadotropin dissociation
Identifieur interne : 000318 ( Istex/Curation ); précédent : 000317; suivant : 000319A study of salmon ( Oncorhynchus tschawytscha ) pituitary gonadotropin dissociation
Auteurs : B. Breton [France]Source :
- General and Comparative Endocrinology [ 0016-6480 ] ; 1981.
Abstract
Urea (8 M) treatment of salmon gonadotropin results in the dissociation of the hormone into two subunits. These subunits were separated using DEAE-cellulose chromatography and gel filtration on Ultrogel ACA 54, and studied for their molecular weights, electrophoretic, biological, and immunological properties. Molecular weights of the α and β subunits were, respectively, 12,500 and 17,000 as determined by gel filtration and sodium dodecyl sulfate-gel electrophoresis. In anionic polyacrylamide gel electrophoresis, 7.5%, the α subunit, migrated more rapidly (Rf = 0.67) than the native hormone s-GtH (Rf = 0.38), and the β subunit did not migrate. The biological activities of the α and β subunits were less than 10% of the GtH. Reassociation allowed a 30% recovery of the initial biological activity. The immunological properties studied on two radioimmunological systems specifically directed against s- and cGtH, show that immunological determinants were connected with the β subunit, which also possesses characteristics of zoological specificity.
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DOI: 10.1016/0016-6480(81)90098-8
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<front><div type="abstract" xml:lang="en">Urea (8 M) treatment of salmon gonadotropin results in the dissociation of the hormone into two subunits. These subunits were separated using DEAE-cellulose chromatography and gel filtration on Ultrogel ACA 54, and studied for their molecular weights, electrophoretic, biological, and immunological properties. Molecular weights of the α and β subunits were, respectively, 12,500 and 17,000 as determined by gel filtration and sodium dodecyl sulfate-gel electrophoresis. In anionic polyacrylamide gel electrophoresis, 7.5%, the α subunit, migrated more rapidly (Rf = 0.67) than the native hormone s-GtH (Rf = 0.38), and the β subunit did not migrate. The biological activities of the α and β subunits were less than 10% of the GtH. Reassociation allowed a 30% recovery of the initial biological activity. The immunological properties studied on two radioimmunological systems specifically directed against s- and cGtH, show that immunological determinants were connected with the β subunit, which also possesses characteristics of zoological specificity.</div>
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